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Title: Implementation of protein design in self-assembling nanostructures
Authors: Maziar Soleymani Ardejani
Keywords: DRNTU::Science::Biological sciences::Biochemistry
Issue Date: 2014
Abstract: The scarcity of predictive design approaches for the rational manipulation of self-assembly, especially that of nanostructured protein complexes poses a bottleneck to the development and technological applicability of this class of materials. Themed around the rational design of protein-protein interactions, this thesis describes the implementation and evaluation of state-of-the-art methodologies for the engineering of a protein nanostructure. In chapter two, we describe a hybrid computational method incorporating topographic analysis of protein surfaces, phylogenic analysis and free energy calculations of protein-protein interactions in protein nanocages. Using this method, we were able to thermally stabilize the protein, but this enhancement in stability did not correlate to a population increase in the cage form. We attribute this observation to the stabilization of a dimer state that is incongruent with cage formation in analogy to an architectural keystone with a shape inappropriate for arch construction. In chapter three, we apply this method to the bacterioferritin with the aim of controlling its nanocage/dimer oligomerization dimorphism in solution. Our results confirm that computational redesign of this dimorphic protein at the C3-symmetrical interfaces forces it to assemble into a nanocage structure that is not only monomorphic but also at least 20°C more stable than the parent. This success proves that the development of such approaches adds to the toolkit of bottom-up molecular design with applications in protein engineering and hybrid nano-materials. In the last chapter, we extend the protein design approach for making non-covalent protein-protein connectors that can direct the self-assembly of large protein complexes (e.g. ferritins) to form nanostructured lattices.
Schools: School of Physical and Mathematical Sciences 
Fulltext Permission: restricted
Fulltext Availability: With Fulltext
Appears in Collections:SPMS Theses

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